PDBsum entry 1cqe

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
552 a.a. *
BOG ×5
HEM ×2
FLP ×2
Waters ×130
* Residue conservation analysis

References listed in PDB file
Key reference
Title The X-Ray crystal structure of the membrane protein prostaglandin h2 synthase-1.
Authors D.Picot, P.J.Loll, R.M.Garavito.
Ref. Nature, 1994, 367, 243-249. [DOI no: 10.1038/367243a0]
PubMed id 8121489
The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 A resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein.
Secondary reference #1
Title Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the prostaglandin h2 synthase cyclooxygenase active site.
Authors P.J.Loll, D.Picot, O.Ekabo, R.M.Garavito.
Ref. Biochemistry, 1996, 35, 7330-7340. [DOI no: 10.1021/bi952776w]
PubMed id 8652509
Full text Abstract
Secondary reference #2
Title The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin h2 synthase.
Authors P.J.Loll, D.Picot, R.M.Garavito.
Ref. Nat Struct Biol, 1995, 2, 637-643.
PubMed id 7552725
Secondary reference #3
Title X-Ray crystal structure of canine myeloperoxidase at 3 a resolution.
Authors J.Zeng, R.E.Fenna.
Ref. J Mol Biol, 1992, 226, 185-207. [DOI no: 10.1016/0022-2836(92)90133-5]
PubMed id 1320128
Full text Abstract
Figure 2.
Figure 2. Stereo photograph showing te averaged electron density ma on the proximal side of the heme. Residues R333, Y334 G335, H336, T337, L338 and 1339 are located in helix H8 and include histidine 336, which provides the proximal ligand to the heme iron. The carboxl group of glutamate 242 can be .seen to occupy electron density that is continuous-with that of the heme macrocycle
Figure 4.
Figure 4. tereo photograph of the averaged electon density map corresponding to the first 2 N-acetylglucosamine (NAG) residues attached to Asn317. The orientations f both sugar molecules are clearly defined by density corresponding to the N-acetyl groups. From the C5 position of the 1st sugr, electron density (not shown) corresponding to t,he l-6 linked fucose projcts backwards.
The above figures are reproduced from the cited reference with permission from Elsevier
Go to PROCHECK summary